Citation

Reboud-Ravaux M, Vilain AC, Boggetto N, Maillard J, Favreau C, Xie J, Mazaleyrat JP, Wakselman M. Biochem. Biophys. Res. Commun. 1991; 178(1): 352-359.

Copyright

(Copyright © 1991, Academic Press)

DOI

10.1016/0006-291x(91)91821-s

PMID

1829886

Abstract

c[Arg-aB-(CH2+SCH3 phi)-Gly4] was designed and studied as a mechanism-based inactivator (suicide substrate) for plasminogen activators (u-PA and t-PA) and plasmin. This compound inhibited u-PA and fulfills criteria expected for the involvement of an enzyme-activated inhibitor: first-order and irreversible process, saturation kinetics, protection by substrate. The limiting first-order rate constant kinact and the apparent enzyme-inhibitor dissociation constant KI were 0.021 s-1 and 9 microM, respectively at pH 7.5 and 25 degrees C. The activation of plasminogen by u-PA is compromised after this enzyme has been treated by the reagent. Plasmin and t-PA were inactivated 40- and 2330-fold less efficiently than u-PA, respectively.

Language: en

Keywords

Amino Acid Sequence; Binding Sites; Enzyme Precursors; Fibrinolysin; Humans; Kinetics; Molecular Sequence Data; Peptides, Cyclic; Plasminogen Activators; Plasminogen Inactivators; Tissue Plasminogen Activator; Urokinase-Type Plasminogen Activator